Two-phase aqueous micellar systems: an alternative method for protein purification

• Autor(a) principal: Rangel-Yagui,C. O.
• Data de Publicação: 2004
• Outros Autores: Pessoa-Jr,A., Blankschtein,D.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Chemical Engineering
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322004000400003
• topic: two-phase aqueous micellar systems; protein purification; excluded-volume interactions; electrostatic interactions

Two-phase aqueous micellar systems can be exploited in separation science for the extraction/purification of desired biomolecules. This article reviews recent experimental and theoretical work by Blankschtein and co-workers on the use of two-phase aqueous micellar systems for the separation of hydrophilic proteins. The experimental partitioning behavior of the enzyme glucose-6-phosphate dehydrogenase (G6PD) in two-phase aqueous micellar systems is also reviewed and new results are presented. Specifically, we discuss very recent work on the purification of G6PD using: i) a two-phase aqueous micellar system composed of the nonionic surfactant n-decyl tetra(ethylene oxide) (C10E4), and (ii) a two-phase aqueous mixed micellar system composed of C10E4 and the cationic surfactant decyltrimethylammonium bromide (C10TAB). Our results indicate that the two-phase aqueous mixed (C10E4/C10TAB) micellar system can improve significantly the partitioning behavior of G6PD relative to that observed in the two-phase aqueous C10E4 micellar system.